VATH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VATH_HUMAN
• UniProt AC: Q9UI12
• Protein Name: V-type proton ATPase subunit H
• Gene Name: ATP6V1H
• Organism: Homo sapiens (Human).
• Sequence Length: 483
• Protein Description: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes..
• Protein Sequence: MTKMDIRGAVDAAVPTNIIAAKAAEVRANKVNWQSYLQGQMISAEDCEFIQRFEMKRSPEEKQEMLQTEGSQCAKTFINLMTHICKEQTVQYILTMVDDMLQENHQRVSIFFDYARCSKNTAWPYFLPMLNRQDPFTVHMAARIIAKLAAWGKELMEGSDLNYYFNWIKTQLSSQKLRGSGVAVETGTVSSSDSSQYVQCVAGCLQLMLRVNEYRFAWVEADGVNCIMGVLSNKCGFQLQYQMIFSIWLLAFSPQMCEHLRRYNIIPVLSDILQESVKEKVTRIILAAFRNFLEKSTERETRQEYALAMIQCKVLKQLENLEQQKYDDEDISEDIKFLLEKLGESVQDLSSFDEYSSELKSGRLEWSPVHKSEKFWRENAVRLNEKNYELLKILTKLLEVSDDPQVLAVAAHDVGEYVRHYPRGKRVIEQLGGKQLVMNHMHHEDQQVRYNALLAVQKLMVHNWEYLGKQLQSEQPQTAAARS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Phosphorylation	AVDAAVPTNIIAAKA CCCCCCCCCHHHHHH	32.24	21406692
22	Ubiquitination	PTNIIAAKAAEVRAN CCCHHHHHHHHHHHC	38.82	21906983
22 (in isoform 1)	Ubiquitination	-	38.82	21890473
22 (in isoform 2)	Ubiquitination	-	38.82	21890473
62	Ubiquitination	MKRSPEEKQEMLQTE CCCCHHHHHHHHHCC	50.31	-
68	Phosphorylation	EKQEMLQTEGSQCAK HHHHHHHCCHHHHHH	38.05	30619164
71	Phosphorylation	EMLQTEGSQCAKTFI HHHHCCHHHHHHHHH	18.82	30619164
176	Ubiquitination	KTQLSSQKLRGSGVA HHHHHCCCCCCCCEE	41.94	-
263	Phosphorylation	MCEHLRRYNIIPVLS HHHHHHHCCHHHHHH	12.32	29978859
270	Phosphorylation	YNIIPVLSDILQESV CCHHHHHHHHHHHHH	23.88	29978859
295	2-Hydroxyisobutyrylation	AFRNFLEKSTERETR HHHHHHHHHCCHHHH	65.90	-
296	Phosphorylation	FRNFLEKSTERETRQ HHHHHHHHCCHHHHH	26.56	22817900
297	Phosphorylation	RNFLEKSTERETRQE HHHHHHHCCHHHHHH	50.56	22817900
307 (in isoform 2)	Ubiquitination	-	3.04	21890473
313	Ubiquitination	ALAMIQCKVLKQLEN HHHHHHHHHHHHHHC	33.94	-
316	Ubiquitination	MIQCKVLKQLENLEQ HHHHHHHHHHHCHHH	56.69	-
316	Acetylation	MIQCKVLKQLENLEQ HHHHHHHHHHHCHHH	56.69	26051181
323 (in isoform 2)	Ubiquitination	-	48.51	-
325 (in isoform 1)	Ubiquitination	-	50.79	21890473
325	Ubiquitination	LENLEQQKYDDEDIS HHCHHHCCCCCCCHH	50.79	21906983
341	Ubiquitination	DIKFLLEKLGESVQD HHHHHHHHHCHHHHH	62.86	-
342 (in isoform 2)	Ubiquitination	-	7.22	21890473
350	Phosphorylation	GESVQDLSSFDEYSS CHHHHHHHCHHHHHH	36.93	24076635
351	Phosphorylation	ESVQDLSSFDEYSSE HHHHHHHCHHHHHHH	43.97	24076635
360 (in isoform 1)	Ubiquitination	-	46.98	21890473
360	Ubiquitination	DEYSSELKSGRLEWS HHHHHHHHCCCCCCC	46.98	21906983
367	Phosphorylation	KSGRLEWSPVHKSEK HCCCCCCCCCCCCHH	13.99	25159151
371	Ubiquitination	LEWSPVHKSEKFWRE CCCCCCCCCHHHHHH	61.62	-
374	Ubiquitination	SPVHKSEKFWRENAV CCCCCCHHHHHHHCH	58.27	-
378 (in isoform 2)	Ubiquitination	-	39.89	21890473
386	Ubiquitination	NAVRLNEKNYELLKI HCHHHCHHHHHHHHH	64.85	-
388	Phosphorylation	VRLNEKNYELLKILT HHHCHHHHHHHHHHH	21.01	22817900
396	Ubiquitination	ELLKILTKLLEVSDD HHHHHHHHHHHCCCC	47.86	21890473
396 (in isoform 1)	Ubiquitination	-	47.86	21890473
438	Sulfoxidation	LGGKQLVMNHMHHED HCCEEEECCCCCCCC	3.76	30846556
441	Sulfoxidation	KQLVMNHMHHEDQQV EEEECCCCCCCCHHH	2.68	30846556
451 (in isoform 2)	Ubiquitination	-	17.34	21890473
465 (in isoform 2)	Phosphorylation	-	35.88	-
466	Phosphorylation	LMVHNWEYLGKQLQS HHHCCHHHHHHHHHC	16.63	27642862
469 (in isoform 1)	Ubiquitination	-	45.28	21890473
469	Ubiquitination	HNWEYLGKQLQSEQP CCHHHHHHHHHCCCC	45.28	21890473
473	Phosphorylation	YLGKQLQSEQPQTAA HHHHHHHCCCCCCHH	46.95	26471730
478	Phosphorylation	LQSEQPQTAAARS-- HHCCCCCCHHHCC--	25.58	29514088
483	Phosphorylation	PQTAAARS------- CCCHHHCC-------	39.59	25159151

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of VATH_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VATH_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of VATH_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VATE1_HUMAN	ATP6V1E1	physical	12163484
VDAC2_HUMAN	VDAC2	physical	22939629
VDAC3_HUMAN	VDAC3	physical	22939629
ZFAN5_HUMAN	ZFAND5	physical	22939629
VINEX_HUMAN	SORBS3	physical	22939629
SOX9_HUMAN	SOX9	physical	21988832
TANK_HUMAN	TANK	physical	21988832
ARMT1_HUMAN	C6orf211	physical	26344197
VA0D1_HUMAN	ATP6V0D1	physical	26344197
VATA_HUMAN	ATP6V1A	physical	26344197
VATF_HUMAN	ATP6V1F	physical	26344197
CDC42_HUMAN	CDC42	physical	26344197
HCD2_HUMAN	HSD17B10	physical	26344197
STMN1_HUMAN	STMN1	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND MASSSPECTROMETRY.
PubMed: 18691976